Reaction Mechanism of Mammalian Mitochondrial Cytochrome c Oxidase

  • Shinya Yoshikawa
  • Kazumasa Muramoto
  • Kyoko Shinzawa-Itoh
Chapter
Part of the Advances in Experimental Medicine and Biology book series (volume 748)

Abstract

Cytochrome c oxidase (COX) is the terminal oxidase of the mitochondrial respiratory system. This enzyme reduces molecular oxygen (O2) to water in a reaction coupled with the pumping of protons across the mitochondrial inner membrane. Progress in investigating the reaction mechanism of this enzyme has been limited by the resolution of its X-ray structure. Bovine heart COX has provided the highest resolution (1.8 Å) X-ray structure presently available among the terminal oxidases. The reaction mechanism of the bovine heart enzyme has been the most extensively studied, particularly with respect to (1) the reduction of O2 to water without release of reactive oxygen species, (2) the mechanism of coupling between the O2 reduction process and proton pumping, (3) the structural basis for unidirectional proton transfer (proton pumping), and (4) the effective prevention of proton leakage from the proton-pumping pathway to the proton pathway used for generation of water molecules. In this chapter, we will review recent structural studies of bovine heart COX and discuss the mechanisms described earlier in context of the structural data.

Notes

Acknowledgments

This work is supported in part by the Grant-in-Aid for Scientific Research 2247012 (S.Y.), the Targeted Protein Research Program, and the Global Center of Excellence Program, each provided by the Japanese Ministry of Education, Culture, Sports, Science and Technology. S.Y. is a Senior Visiting Scientist in the RIKEN Harima Institute.

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Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  • Shinya Yoshikawa
    • 1
  • Kazumasa Muramoto
    • 1
  • Kyoko Shinzawa-Itoh
    • 1
  1. 1.Department of Life ScienceUniversity of HyogoHyogoJapan

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